The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E + SES →→E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km Almost all active sites are empty. The rate is half of the maximum rate. [S] = Km Answer Bank Increasing [Etotal] will increase Km. [S] >> Km [ES] is much higher than [Efree). This condition rarely occurs for most in vivo enzymes. Not true for any of these conditions The rate is directly proportional to [S].
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E + SES →→E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km Almost all active sites are empty. The rate is half of the maximum rate. [S] = Km Answer Bank Increasing [Etotal] will increase Km. [S] >> Km [ES] is much higher than [Efree). This condition rarely occurs for most in vivo enzymes. Not true for any of these conditions The rate is directly proportional to [S].
Chemistry
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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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![The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an
enzyme-catalyzed, single-substrate reaction E + SES →→ E + P. The model can be more readily understood when
comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km.
Match each statement with the condition that it describes.
Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme
concentration and [Efree] refers to the concentration of free enzyme.
[S] << Km
Almost all active sites are empty.
The rate is half of the maximum rate.
[S] =
Km
Answer Bank
Increasing [Etotal] will increase Km.
[S] >> Km
[ES] is much higher than [Efree].
This condition rarely occurs for most in vivo enzymes.
Not true for any of these
conditions
The rate is directly proportional to [S].](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fbfa5cafe-7ecb-4c60-949b-230a1714b526%2F5baec1ce-5532-4630-81b5-cb89fcca637f%2Fzbehhj_processed.jpeg&w=3840&q=75)
Transcribed Image Text:The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an
enzyme-catalyzed, single-substrate reaction E + SES →→ E + P. The model can be more readily understood when
comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km.
Match each statement with the condition that it describes.
Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme
concentration and [Efree] refers to the concentration of free enzyme.
[S] << Km
Almost all active sites are empty.
The rate is half of the maximum rate.
[S] =
Km
Answer Bank
Increasing [Etotal] will increase Km.
[S] >> Km
[ES] is much higher than [Efree].
This condition rarely occurs for most in vivo enzymes.
Not true for any of these
conditions
The rate is directly proportional to [S].
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